2ybg

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[[Image:2ybg.png|left|200px]]
 
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==Structure of Lys120-acetylated p53 core domain==
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The line below this paragraph, containing "STRUCTURE_2ybg", creates the "Structure Box" on the page.
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<StructureSection load='2ybg' size='340' side='right'caption='[[2ybg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ybg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YBG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2ybg| PDB=2ybg | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ybg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybg OCA], [https://pdbe.org/2ybg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ybg RCSB], [https://www.ebi.ac.uk/pdbsum/2ybg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ybg ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lys120 in the DNA-binding domain (DBD) of p53 becomes acetylated in response to DNA damage. But, the role and effects of acetylation are obscure. We prepared p53 specifically acetylated at Lys120, AcK120p53, by in vivo incorporation of acetylated lysine to study biophysical and structural consequences of acetylation that may shed light on its biological role. Acetylation had no affect on the overall crystal structure of the DBD at 1.9-A resolution, but significantly altered the effects of salt concentration on specificity of DNA binding. p53 binds DNA randomly in vitro at effective physiological salt concentration and does not bind specifically to DNA or distinguish among its different response elements until higher salt concentrations. But, on acetylation, AcK120p53 exhibited specific DNA binding and discriminated among response elements at effective physiological salt concentration. AcK120p53 and p53 had the highest affinity to the same DNA sequence, although acetylation reduced the importance of the consensus C and G at positions 4 and 7, respectively. Mass spectrometry of p53 and AcK120p53 DBDs bound to DNA showed they preferentially segregated into complexes that were either DNA(p53DBD)(4) or DNA(AcK120DBD)(4), indicating that the different DBDs prefer different quaternary structures. These results are consistent with electron microscopy observations that p53 binds to nonspecific DNA in different, relaxed, quaternary states from those bound to specific sequences. Evidence is accumulating that p53 can be sequestered by random DNA, and target search requires acetylation of Lys120 and/or interaction with other factors to impose specificity of binding via modulating changes in quaternary structure.
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===STRUCTURE OF LYS120-ACETYLATED P53 CORE DOMAIN===
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Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration.,Arbely E, Natan E, Brandt T, Allen MD, Veprintsev DB, Robinson CV, Chin JW, Joerger AC, Fersht AR Proc Natl Acad Sci U S A. 2011 May 17;108(20):8251-6. Epub 2011 Apr 27. PMID:21525412<ref>PMID:21525412</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ybg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21525412}}, adds the Publication Abstract to the page
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*[[P53 3D structures|P53 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21525412 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21525412}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2ybg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBG OCA].
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==Reference==
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<ref group="xtra">PMID:021525412</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Allen, M D.]]
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[[Category: Large Structures]]
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[[Category: Arbely, E.]]
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[[Category: Allen MD]]
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[[Category: Fersht, A R.]]
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[[Category: Arbely E]]
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[[Category: Joerger, A C.]]
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[[Category: Fersht AR]]
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[[Category: Joerger AC]]

Current revision

Structure of Lys120-acetylated p53 core domain

PDB ID 2ybg

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